Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP).
ERM proteins play a role in the cross-linking found between plasma membranes and actin filaments. The N-terminal FERM domains of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. During cell migration and movement, membrane-type 1 matrix metalloproteinase (MT1-MMP) on plasma membranes sheds adhesion molecule CD44 in addition to degrading the extracellular matrix. Here, the interaction between the radixin FERM domain and the MT1-MMP cytoplasmic tail is reported and preliminary crystallographic characterization of crystals of the radixin FERM domain bound to the cytoplasmic tail of MT1-MMP is presented. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 122.7, c = 128.3 A, and contain one complex in the crystallographic asymmetric unit. The diffraction data were collected to a resolution of 2.4 A.
Terawaki
Shin-ichi
S
Structural Biology Laboratory, Nara Institute of Science and Technology, Keihanna Science City, Nara 630-0192, Japan.
Kitano
Ken
K
Aoyama
Miki
M
Hakoshima
Toshio
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D020781:Matrix Metalloproteinase 1 / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D011485:Protein Binding; D014961:X-Ray Diffraction
D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009842:Oligopeptides; C071776:radixin; D020781:Matrix Metalloproteinase 1